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Fuse, S., Tsukamoto, H., Yuan, Y., Wang, T. - S. Andrew, Zhang, Y., Bolla, M., Walker, S., Sliz, P., and Kahne, D. (2010) Functional and structural analysis of a key region of the cell wall inhibitor moenomycin. ACS Chem Biol. 5, 701-11
Funk, M. A. (2015) Structural Studies of Radical Enzymes in Bacterial Central Metabolism. Ph.D. thesis, Massachusetts Institute of Technology, Cambridge, Massachusetts
Funk, M. A., Judd, E. T., E Marsh, N. G., Elliott, S. J., and Drennan, C. L. (2014) Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity. Proc Natl Acad Sci U S A. 111, 10161-6
Fu, T. - M., Li, Y., Lu, A., Li, Z., Vajjhala, P. R., Cruz, A. C., Srivastava, D. B., DiMaio, F., Penczek, P. A., Siegel, R. M., Stacey, K. J., Egelman, E. H., and Wu, H. (2016) Cryo-EM Structure of Caspase-8 Tandem DED Filament Reveals Assembly and Regulation Mechanisms of the Death-Inducing Signaling Complex. Mol Cell. 64, 236-250
Fritschi, C. J., Liang, S., Mohammadi, M., Anang, S., Moraca, F., Chen, J., Madani, N., Sodroski, J. G., Abrams, C. F., Hendrickson, W. A., and Smith, A. B. (2021) Identification of gp120 Residue His105 as a Novel Target for HIV-1 Neutralization by Small-Molecule CD4-Mimics. ACS Med Chem Lett. 12, 1824-1831
Fribourgh, J. L., Nguyen, H. C., Matreyek, K. A., Alvarez, F. Joan D., Summers, B. J., Dewdney, T. G., Aiken, C., Zhang, P., Engelman, A., and Xiong, Y. (2014) Structural insight into HIV-1 restriction by MxB. Cell Host Microbe. 16, 627-638
Frey, K. M., Bertoletti, N., Chan, A. H., Ippolito, J. A., Bollini, M., Spasov, K. A., Jorgensen, W. L., and Anderson, K. S. (2022) Structural Studies and Structure Activity Relationships for Novel Computationally Designed Non-nucleoside Inhibitors and Their Interactions With HIV-1 Reverse Transcriptase. Front Mol Biosci. 9, 805187
Frey, G., Chen, J., Rits-Volloch, S., Freeman, M. M., Zolla-Pazner, S., and Chen, B. (2010) Distinct conformational states of HIV-1 gp41 are recognized by neutralizing and non-neutralizing antibodies. Nat Struct Mol Biol. 17, 1486-91
French, J. B., Yates, P. A., D Soysa, R., Boitz, J. M., Carter, N. S., Chang, B., Ullman, B., and Ealick, S. E. (2011) The Leishmania donovani UMP synthase is essential for promastigote viability and has an unusual tetrameric structure that exhibits substrate-controlled oligomerization. J Biol Chem. 286, 20930-41
French, J. B., Cen, Y., Sauve, A. A., and Ealick, S. E. (2010) High-resolution crystal structures of Streptococcus pneumoniae nicotinamidase with trapped intermediates provide insights into the catalytic mechanism and inhibition by aldehydes . Biochemistry. 49, 8803-12
French, J. B., Neau, D. B., and Ealick, S. E. (2011) Characterization of the structure and function of Klebsiella pneumoniae allantoin racemase. J Mol Biol. 410, 447-60
French, J. B., and Ealick, S. E. (2011) Structural and kinetic insights into the mechanism of 5-hydroxyisourate hydrolase from Klebsiella pneumoniae. Acta Crystallogr D Biol Crystallogr. 67, 671-7
French, J. B., Begley, T. P., and Ealick, S. E. (2011) Structure of trifunctional THI20 from yeast. Acta Crystallogr D Biol Crystallogr. 67, 784-91
French, J. B., and Ealick, S. E. (2010) Structural and mechanistic studies on Klebsiella pneumoniae 2-Oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase. J Biol Chem. 285, 35446-54
French, J. B., and Ealick, S. E. (2010) Biochemical and structural characterization of a ureidoglycine aminotransferase in the Klebsiella pneumoniae uric acid catabolic pathway. Biochemistry. 49, 5975-7
Freeman, M. M., Seaman, M. S., Rits-Volloch, S., Hong, X., Kao, C. - Y., Ho, D. D., and Chen, B. (2010) Crystal structure of HIV-1 primary receptor CD4 in complex with a potent antiviral antibody. Structure. 18, 1632-41
Fraser, B. J., Beldar, S., Seitova, A., Hutchinson, A., Mannar, D., Li, Y., Kwon, D., Tan, R., Wilson, R. P., Leopold, K., Subramaniam, S., Halabelian, L., Arrowsmith, C. H., and Bénard, F. (2022) Structure and activity of human TMPRSS2 protease implicated in SARS-CoV-2 activation. Nat Chem Biol. 10.1038/s41589-022-01059-7
Frappier, V., Jenson, J. M., Zhou, J., Grigoryan, G., and Keating, A. E. (2019) Tertiary Structural Motif Sequence Statistics Enable Facile Prediction and Design of Peptides that Bind Anti-apoptotic Bfl-1 and Mcl-1. Structure. 10.1016/j.str.2019.01.008
Foster, B. M., Rosenberg, D., Salvo, H., Stephens, K. L., Bintz, B. J., Hammel, M., Ellenberger, T., Gainey, M. D., and Wallen, J. R. (2019) Combined Solution and Crystal Methods Reveal the Electrostatic Tethers That Provide a Flexible Platform for Replication Activities in the Bacteriophage T7 Replisome. Biochemistry. 58, 4466-4479
Fortinez, C. Marie, Bloudoff, K., Harrigan, C., Sharon, I., Strauss, M., and T Schmeing, M. (2022) Structures and function of a tailoring oxidase in complex with a nonribosomal peptide synthetase module. Nat Commun. 13, 548
G Forse, J., Ram, N., D Banatao, R., Cascio, D., Sawaya, M. R., Klock, H. E., Lesley, S. A., and Yeates, T. O. (2011) Synthetic symmetrization in the crystallization and structure determination of CelA from Thermotoga maritima. Protein Sci. 20, 168-78
Fontán, L., Qiao, Q., Hatcher, J. M., Casalena, G., Us, I., Teater, M., Durant, M., Du, G., Xia, M., Bilchuk, N., Chennamadhavuni, S., Palladino, G., Inghirami, G., Philippar, U., Wu, H., Scott, D. A., Gray, N. S., and Melnick, A. (2018) Specific covalent inhibition of MALT1 paracaspase suppresses B cell lymphoma growth. J Clin Invest. 128, 4397-4412
Fisher, O. S., Deng, H., Liu, D., Zhang, Y., Wei, R., Deng, Y., Zhang, F., Louvi, A., Turk, B. E., Boggon, T. J., and Su, B. (2015) Structure and vascular function of MEKK3-cerebral cavernous malformations 2 complex. Nat Commun. 6, 7937
Fisher, O. S., Zhang, R., Li, X., Murphy, J. W., Demeler, B., and Boggon, T. J. (2013) Structural studies of cerebral cavernous malformations 2 (CCM2) reveal a folded helical domain at its C-terminus. FEBS Lett. 587, 272-7
Fisher, O. S., Liu, W., Zhang, R., Stiegler, A. L., Ghedia, S., Weber, J. L., and Boggon, T. J. (2015) Structural basis for the disruption of the cerebral cavernous malformations 2 (CCM2) interaction with Krev interaction trapped 1 (KRIT1) by disease-associated mutations. J Biol Chem. 290, 2842-53